Evidence map›Paper›PMID 21070971›Full record

ArticleMolecular cell2010

An E3 ubiquitin ligase prevents ectopic localization of the centromeric histone H3 variant via the centromere targeting domain.

Prerana Ranjitkar, Maximilian O Press, Xianhua Yi, Richard Baker, Michael J MacCoss, Sue Biggins

Abstract read
In one paragraph

Article in Molecular cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 132 papers.

0numbers the graph read from it
0cells of the map it votes in
132citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

132 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Preserving centromere identity: right amounts of CENP-A at the right place and time.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2025
    Review
  5. Review
  6. Article
  7. Article
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  10. Article
  11. Article
  12. Article
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  14. Article
  15. Article
  16. Article
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  18. SUMO control of centromere homeostasis.Frontiers in cell and developmental biology · 2023
    Review
  19. Article
  20. Article

72 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors.

Prerana RanjitkarDivision of Basic Sciences, Fred Hutchinson Cancer Research Center, 1100 Fairview Avenue N., P.O. Box 19024, Seattle, WA 98109, USA.
Maximilian O Press
Xianhua Yi
Richard Baker
Michael J MacCoss
Sue Biggins

Funding

ZDS2P REGULATES SWE1P-DEPENDENT POLARIZED CELL GROWTH IN S CEREVISIAEP41RR011823 · NCRR · UNIVERSITY OF WASHINGTON · PI DAVIS, TRACY · 1996 to 2011
$24.7M
Chromosome Metabolism and Cancer Training GrantT32CA009657 · NCI · FRED HUTCHINSON CANCER RESEARCH CENTER · PI EISENMAN, ROBERT NEIL · 1991 to 2020
$7.6M
Regulation of Centromeric ChromatinR01GM078069 · NIGMS · FRED HUTCHINSON CANCER RESEARCH CENTER · PI BIGGINS, SUSAN · 2007 to 2015
$2.7M
NCI NIH HHS NCI 5 T32 CA09657NCI NIH HHS T32 CA009657NCRR NIH HHS P41 RR011823NCRR NIH HHS RR011823NIGMS NIH HHS R01 GM078069
6 · The paper itself

Abstract

Proper centromere function is critical to maintain genomic stability and to prevent aneuploidy, a hallmark of tumors and birth defects. A conserved feature of all eukaryotic centromeres is an essential histone H3 variant called CENP-A that requires a centromere targeting domain (CATD) for its localization. Although proteolysis prevents CENP-A from mislocalizing to euchromatin, regulatory factors have not been identified. Here, we identify an E3 ubiquitin ligase called Psh1 that leads to the degradation of Cse4, the budding yeast CENP-A homolog. Cse4 overexpression is toxic to psh1Δ cells and results in euchromatic localization. Strikingly, the Cse4 CATD is a key regulator of its stability and helps Psh1 discriminate Cse4 from histone H3. Taken together, we propose that the CATD has a previously unknown role in maintaining the exclusive localization of Cse4 by preventing its mislocalization to euchromatin via Psh1-mediated degradation.

Indexed as

Amino Acid SequenceCentromereChromosomal Proteins, Non-HistoneDNA-Binding ProteinsEuchromatinHistonesMolecular Sequence DataMutationPeptide Elongation FactorsProtein BindingProtein IsoformsProtein Processing, Post-TranslationalProtein StabilityProtein Structure, TertiaryProtein TransportSaccharomyces cerevisiaeChromosomal Proteins, Non-HistoneCSE4 protein, S cerevisiaeDNA-Binding ProteinsEuchromatinHistonesPeptide Elongation FactorsProtein IsoformsPsh1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitin-Protein Ligases

Identifiers

PMID21070971
PMCPMC2995698

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.